A0A5F9C0Q4 · A0A5F9C0Q4_RABIT

Function

function

Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)-octadecenoylglycerol + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2,3-tributanoylglycerol + H2O = dibutanoylglycerol + butanoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z-octadecenoyl)-sn-glycero-3-phosphocholine + (9Z)-octadecenoate + H+
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H+
    This reaction proceeds in the forward direction.
  • a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
    EC:3.1.1.32 (UniProtKB | ENZYME | Rhea)
  • a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H+
    EC:3.1.1.34 (UniProtKB | ENZYME | Rhea)

GO annotations

AspectTerm
Cellular Componentchylomicron
Cellular Componentplasma membrane
Cellular Componentvery-low-density lipoprotein particle
Molecular Function1-acyl-2-lysophosphatidylserine acylhydrolase activity
Molecular Functionapolipoprotein binding
Molecular Functionheparin binding
Molecular Functionlipoprotein lipase activity
Molecular Functionphosphatidylserine 1-acylhydrolase activity
Molecular Functionphospholipase A1 activity
Biological Processfatty acid biosynthetic process
Biological Processtriglyceride catabolic process
Biological Processvery-low-density lipoprotein particle remodeling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipoprotein lipase
  • EC number
  • Short names
    LPL

Gene names

    • Name
      LPL

Organism names

  • Taxonomic identifier
  • Strain
    • Thorbecke inbred
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    A0A5F9C0Q4

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein
Secreted
Note: Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles.

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-20
ChainPRO_502397666421-497Lipoprotein lipase

Post-translational modification

Tyrosine nitration after lipopolysaccharide (LPS) challenge down-regulates the lipase activity.

Keywords

Expression

Gene expression databases

Interaction

Subunit

Homodimer. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids.
Homodimer. Interacts with GPIHBP1 with 1:1 stoichiometry. Interacts with APOC2; the interaction activates LPL activity in the presence of lipids. Interaction with heparan sulfate proteoglycans is required to protect LPL against loss of activity. Associates with lipoprotein particles in blood plasma. Interacts with LMF1 and SEL1L; interaction with SEL1L is required to prevent aggregation of newly synthesized LPL in the endoplasmic reticulum (ER), and for normal export of LPL from the ER to the extracellular space. Interacts with SORL1; SORL1 acts as a sorting receptor, promoting LPL localization to endosomes and later to lysosomes, leading to degradation of newly synthesized LPL.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain340-458PLAT

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    497
  • Mass (Da)
    55,333
  • Last updated
    2019-12-11 v1
  • Checksum
    5A977E25865AD2BE
MESKTLLLVVLGAWLQSLTASRGGVAAADRNDFLDIETKFALRTPEDTADDTCHLVPGVVESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLLRAQQHYPVSAGYTKLVGKDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNRKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQQPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCTSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRAQMPYKVFHYQVKIHFSGTESQTQTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWNSDSYFSWADWWGSPSFTIAKIRGVPDLRHPCVLRLEKRFQNMTQTNASNSCSVLVVVAFGGTSFSGNLEERGLLPGLAGDQVHICEEV

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
D5FIT0D5FIT0_RABITLPL474

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAGW02066180
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAGW02066181
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAGW02066182
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AAGW02066183
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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